ID   GLRX2_ECOL6             Reviewed;         215 AA.
AC   P0AC60; P39811; P75928; P77043;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Glutaredoxin 2;
DE            Short=Grx2;
GN   Name=grxB; OrderedLocusNames=c1331;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Involved in reducing some disulfides in a coupled system with
CC       glutathione reductase. Does not act as hydrogen donor for
CC       ribonucleotide reductase (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN79804.1; -; Genomic_DNA.
DR   RefSeq; WP_000780912.1; NC_004431.1.
DR   AlphaFoldDB; P0AC60; -.
DR   BMRB; P0AC60; -.
DR   SMR; P0AC60; -.
DR   STRING; 199310.c1331; -.
DR   EnsemblBacteria; AAN79804; AAN79804; c1331.
DR   GeneID; 58461742; -.
DR   KEGG; ecc:c1331; -.
DR   eggNOG; COG2999; Bacteria.
DR   HOGENOM; CLU_072939_0_1_6; -.
DR   OMA; GKKMAPI; -.
DR   BioCyc; ECOL199310:C1331-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   CDD; cd03199; GST_C_GRX2; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR007494; Glutaredoxin2_C.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR011901; Grx2.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF04399; Glutaredoxin2_C; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDG01204; Grx2-like.1; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR02182; GRXB; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Electron transport; Redox-active center; Transport.
FT   CHAIN           1..215
FT                   /note="Glutaredoxin 2"
FT                   /id="PRO_0000141587"
FT   DOMAIN          1..77
FT                   /note="GST N-terminal"
FT   DISULFID        9..12
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   215 AA;  24350 MW;  A8AAAB2548D824FE CRC64;
     MKLYIYDHCP YCLKARMIFG LKNIPVELHV LLNDDAETPT RMVGQKQVPI LQKDDSRYMP
     ESMDIVHYVD KLDGKPLLTG KRSPAIEEWL RKVNGYANKL LLPRFAKSAF DEFSTPAARK
     YFVDKKEASA GNFADLLAHS DGLIKNISDD LRALDKLIVK PNAVNGELSE DDIQLFPLLR
     NLTLVAGINW PSRVADYRDN MAKQTQINLL SSMAI